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- W2076758778 abstract "Domain swapping has been shown to be an important mechanism controlling multiprotein assembly and has been suggested recently as a possible mechanism underlying protein aggregation. Understanding oligomerization via domain swapping is therefore of theoretical and practical importance. By using a symmetrized structure-based (Gō) model, we demonstrate that in the free-energy landscape of domain swapping, a large free-energy barrier separates monomeric and domain-swapped dimeric configurations. We investigate the effect of finite monomer concentration, by implementing a new semi-analytical method, which involves computing the second virial coefficient, a thermodynamic indicator of inter-molecular interactions. This method, together with the symmetrized structure-based (Gō) model, minimizes the need for expensive many-protein simulations, providing a convenient framework to investigate concentration effect. Finally, we perform direct simulations of domain-swapped trimer formation, showing that this modeling approach can be used for higher-order oligomers." @default.
- W2076758778 created "2016-06-24" @default.
- W2076758778 creator A5007096444 @default.
- W2076758778 creator A5030987631 @default.
- W2076758778 creator A5036939761 @default.
- W2076758778 date "2005-09-01" @default.
- W2076758778 modified "2023-09-25" @default.
- W2076758778 title "Protein Oligomerization Through Domain Swapping: Role of Inter-molecular Interactions and Protein Concentration" @default.
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- W2076758778 doi "https://doi.org/10.1016/j.jmb.2005.06.062" @default.
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